Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
15
|
| pubmed:dateCreated |
1984-10-12
|
| pubmed:abstractText |
Assignments have been made for 11 methyl, one Gln-C gamma, one Thr-C beta, and all six Tyr-C zeta carbon resonances of ribonuclease A. These partially serve to delineate the binding sites for Cu2+, Mn2+, phosphate, cytidine and its 2'-, 3'-, and 5'-phosphates (Cyd and Cyd-2'-P, -3'-P, and -5'-P), and one or a few urea molecules at low concentration. Evidence is presented for a conformational change, and hence flexibility, in the active site region around the optimum pD for enzymic activity and another such change at around the optimum temperature. The binding of cytidine-containing ligands is shown to have extensive conformational consequences for methyl groups but less for hydrophobic aromatic residues, implying that the former make a special contribution to molecular flexibility. The cytosine ring in Cyd-2'-P, -3'-P, and -5'-P is found to be close but far from parallel to the ring of Phe-120. In contrast to previous claims, ribonuclease A is shown not to unfold even partially before denaturation. On denaturation, it passes to a new but structured state.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
17
|
| pubmed:volume |
23
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
3515-21
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1984
|
| pubmed:articleTitle |
Ribonuclease A: carbon-13 nuclear magnetic resonance assignments, binding sites, and conformational flexibility.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|